SUMO Protease Animal-Free, His
SUMO Protease Animal-Free, His

Lane 1: 2 μg of SUMO Protease Animal-Free, His, non-reducing (NR)
Lane 2: 2 μg of SUMO Protease Animal-Free, His, reducing (R)
> 95% as analyzed by SDS-PAGE

SUMO Protease Animal-Free, His

GenScript’s SUMO Protease Animal-Free, His, is the recombinant SUMO protease fragment from Saccharomyces cerevisiae. . It is produced under an animal free process, and is suitable for drug and vaccine development, manufacture and other applications.
Z03691
¥7,835.00

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Product Introduction
Source Recombinant SUMO Protease expressed in E.coli
Species Saccharomyces cerevisiae
Tag His Tag
Purity ≥ 95% as analyzed by SDS-PAGE
Biological Activity 10 U/μl
Unit Definition One unit of SUMO Protease cleaves ≥ 85% of 2 μg control substrate in 1 h at 30℃
Endotoxin Level < 0.2 EU/μg of protein by gel clotting method
Molecular Weight Predicted MW: 27 kDa
Storage Buffer 25 mM Tris-HCl, 0.1% Igepal (NP-40), 250 mM NaCl, 0.5 mM DTT 50% (v/v) glycerol, pH 8.0
Storage & Stability Upon receiving, the product remains stable for 6 months at -20 °C. This product is stable for 1 week at 37 °C. Avoid repeated freeze-thaw cycles by making single-use aliquots before the solution is stored at -20 °C.

Applications
His Tag

Examples
  • SUMO Protease Animal-Free, His
    • SUMO Protease Animal-Free, His

    Lane 1: 2 μg of SUMO Protease Animal-Free, His, non-reducing (NR)
    Lane 2: 2 μg of SUMO Protease Animal-Free, His, reducing (R)
    > 95% as analyzed by SDS-PAGE


Background
Target Background SUMO protease, also known as Ulp, is a protease that specifically removes small ubiquitin-related modifier (SUMO) in any recombinant SUMO fusion protein. Different from other tag removal proteases such as enterokinase (EK) and TEV which recognize a specific amino acid sequence and cut at a specific cleavage site, SUMO protease recognizes the SUMO tertiary structure and cleave it, more specifically and leaving no residual amino acids.
GenScript’s SUMO Protease Animal-Free, His, is the recombinant SUMO protease fragment from Saccharomyces cerevisiae. This recombinant enzyme is expressed in E.coli and purified to obtain high yields of the active enzyme. It is produced under an animal free process, and is suitable for drug and vaccine development, manufacture and other applications. This product is designed with a C-terminal 6x His tag which can be removed after the SUMO cleavage reaction by purification using Ni2+ affinity chromatography resin (Cat. No. L00223) or Ni-charged magnetic beads (Cat. No. L00295).

For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.